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Aminopeptidase

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'''Aminopeptidases''' catalyze a release of an N-terminal amino acid from a peptide, amide, or arylamide.
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Aminopeptidases catalyze a release of an N-terminal amino acid from a peptide, amide, or arylamide.
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== S. griseus aminopeptidase ==
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<applet load='1xjo' size='500' color='white' frame='true' align='right' />
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''S. griseus'' aminopeptidase (SGAP) cleaves the N-terminal amino acid from a peptide or protein, and is specific for larger hydrophobic acids, especially leucine. No cleavage occurs if the next residue is proline.
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The <scene name='Aminopeptidase/Active_site/1'>active site</scene> of the enzyme contains two Zn2+ ions with His85 and Asp160 as ligands for one ion, and Glu132 and His247 as ligands for the second ion. Asp97 is a common ligand to both ions. What appears to be a phosphate anion is bound to both zinc atoms, replacing the water molecule/hydroxide ion normally found in this class of enzyme.
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Revision as of 18:02, 14 November 2007

Aminopeptidases catalyze a release of an N-terminal amino acid from a peptide, amide, or arylamide.

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, David Canner, Joel L. Sussman, Eran Hodis

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